Issue 40, 2021
From the journal:

Chemical Science

Targeted protein oxidation using a chromophore-modified rapamycin analog†

Taylor M. Courtney, ORCID logo ‡a   Chasity P. Hankinson,‡a   Trevor J. Horsta  and  Alexander Deiters ORCID logo *a  

* Corresponding authors

a Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA
E-mail: deiters@pitt.edu

Abstract

Chemically induced dimerization of FKBP and FRB using rapamycin and rapamycin analogs has been utilized in a variety of biological applications. Formation of the FKBP-rapamycin-FRB ternary complex is typically used to activate a biological process and this interaction has proven to be essentially irreversible. In many cases, it would be beneficial to also have temporal control over deactivating a biological process once it has been initiated. Thus, we developed the first reactive oxygen species-generating rapamycin analog toward this goal. The BODIPY-rapamycin analog BORap is capable of dimerizing FKBP and FRB to form a ternary complex, and upon irradiation with 530 nm light, generates singlet oxygen to oxidize and inactivate proteins of interest fused to FKBP/FRB.

Graphical abstract: Targeted protein oxidation using a chromophore-modified rapamycin analog

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Article information

DOI
https://doi.org/10.1039/D1SC04464H
Article type
Edge Article
Submitted
13 Aug 2021
Accepted
30 Aug 2021
First published
22 Sep 2021
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2021,12, 13425-13433

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Targeted protein oxidation using a chromophore-modified rapamycin analog

T. M. Courtney, C. P. Hankinson, T. J. Horst and A. Deiters, Chem. Sci., 2021, 12, 13425 DOI: 10.1039/D1SC04464H

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